Characterization of AoAA11M: a new copper-dependent lytic polysaccharide monooxygenase for oxidative chitin degradation.

Authors

Yuqi Gao, Jialu Cheng, Luhan Zhang, Minze Zhu, Jifeng Liu, Jiaxing Guo, Jianmin Gao, Lianzhe Wang, Lei Ma, Mengmeng Wang

Published in

Carbohydrate research. Volume 567. Pages 110004. Jun 15, 2026. Epub Jun 15, 2026.

Abstract

Lytic polysaccharide monooxygenases (LPMOs), which are also known as the Auxiliary Activities (AA) family, have drawn a lot of interest because of their potential to help break down biomass. However, the AA11 family remains relatively understudied. In this study, we characterized a novel AA11 family protein, derived from Aspergillus oryzae RIB40, which we named AoAA11 M. Using isothermal titration calorimetry (ITC), electron paramagnetic resonance (EPR), and melting temperature (T_m) analysis, we confirmed that AoAA11 M could bind copper. MALDI-TOF-MS analysis showed that AoAA11 M could act on α-chitin at the C1 position, and also release some deacetylated chitooligosaccharides. When used together with chitinase, AoAA11 M boosted the degradation of α-chitin by 53.3%. Mutagenesis and activity assays pointed to His1, His69, and Tyr131 as key residues for catalytic activity. Our findings expand what we know about the AA11 family and highlight AoAA11 M as a promising biocatalyst for chitin valorization.

PMID:
42320174
Bibliographic data and abstract were imported from PubMed on 20 Jun 2026.

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